ID A0A183BTN1_GLOPA Unreviewed; 1253 AA.
AC A0A183BTN1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Neurexin-4 {ECO:0000313|WBParaSite:GPLIN_000396700};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000396700};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000396700}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A183BTN1; -.
DR WBParaSite; GPLIN_000396700; GPLIN_000396700; GPLIN_000396700.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1131..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..287
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 468..505
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 720..887
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 883..921
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1184..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 495..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1253 AA; 137169 MW; 09AC279D4AF29E1B CRC64;
MVKFGSLHVV RRISPLGAFY LAHFIDEEDA VKEFRHSSLR QRHLTRQANG ELLVIYSGHS
AHSLEWARVD LLASALRLEP LLGGDDVQQH VSPVLLVTAC PAPVLTVPVS LPAPYTFKTR
SSASTDEQQL ISTNISPAYE NELRVNFKTF QNALFLYSVA DYGDHLIVQL AGGRVEVFFD
FGGQQRSQLT GGLALNDGEW HELRWSHHFD TAELFIDGVC MNSTEIGGLY RKLDLHSTME
IGGRPEEIGD EQIVEFSLEN VFYGCLAMME LNGLNLLGSA PKKLPLCQMP QPQLVAIGSR
SVLQIPYSFL PFAFDFHVLL QRPQLQQQRV GAVSGRQHGA EADVALLSIL DTANATLLQL
SIAELDNGAL SIRTSLGTGG QAPRVVTLGG SVARGWHAVV VKLRGGDALE VEMDGRAAYW
VEGPAARHIG KTMHTFLLSA TGCYRSATID LKQGMPIGDE MIPDTCPLVE SCSPNPCQNG
GQCVQNGFAS FSCECQHNYT GRFCHISKLP HSCEEHFASG AVSKRVLIDL DGGGPLQAFI
VECRRKLRSK QDGAIEEVIT IIRHDAPPQG IIVRGQSEPG AVRRILHYGL EEPVLDRLVA
AFDHCGQLMR FQCVGGQRLM HYGAENRPSA WYATRNAQHG LQWGDAPPFS RMCSCALNDS
CAGQRSCNCD SGQDAVDIGT NTHHQLLPIL QLFIGGGTEP NAMANVSIGP LECSRRHVFE
TITFMDRNQR LIASHIFPSA STFHAALSIR LARPQLTVFT YASANHERWF QLFVRAGHLV
GQLVYAGISH ELVSDVVVDD DRWHTVSWEV DELSMRLVVD RAEKTVFAAS VPPRTSVLII
GARTGKDRSG FAGQMRDFRL NGAEVALGQL AQRALGAGVQ LGAWGACEVQ NACHNDGRCV
ELYAAFTCNC SLTPFTGDTC EDEVGMWVPL GSELKIAWQH PAQMSNCYRI SIQSASTGVA
LIRAQALFAE SNFNMSIDRQ GQLNVQIFDG VFFAQKVTLS PRFVVADNKS KDIRFCANST
GLEININGEQ ALMLEGNFTF FSALNSWKFV DPNFSGCIAR LMVGDAFPLK DPRGSRLQHS
GKIRFGSCPY DNLEHRKTQP SLTTTESREH DADLSDIHAT SSNFMKSQRQ LLFITPAIGF
ASALCILLSL CVFLLYIQHR PDGVYKTNER NAFVPIGVGT VGDNKRRHGN VNDYGNAGGS
SRRCTRRSNP PNASTSADGP CITKSSTNFL GGASADQPPP PTSISQYMFD SGL
//
